ROSICS: CHEMISTRY AND PROTEOMICS OF CYSTEINE MODIFICATIONS IN REDOX BIOLOGY

Cited 57 time in webofscience Cited 0 time in scopus
  • Hit : 593
  • Download : 0
Post-translational modifications (PTMs) occurring in proteins determine their functions and regulations. Proteomic tools are available to identify PTMs and have proved invaluable to expanding the inventory of these tools of nature that hold the keys to biological processes. Cysteine (Cys), the least abundant (1-2%) of amino acid residues, are unique in that they play key roles in maintaining stability of protein structure, participating in active sites of enzymes, regulating protein function and binding to metals, among others. Cys residues are major targets of reactive oxygen species (ROS), which are important mediators and modulators of various biological processes. It is therefore necessary to identify the Cys-containing ROS target proteins, as well as the sites and species of their PTMs. Cutting edge proteomic tools which have helped identify the PTMs at reactive Cys residues, have also revealed that Cys residues are modified in numerous ways. These modifications include formation of disulfide, thiosulfinate and thiosulfonate, oxidation to sulfenic, sulfinic, sulfonic acids and thiosulfonic acid, transformation to dehydroalanine (DHA) and serine, palmitoylation and farnesylation, formation of chemical adducts with glutathione, 4-hydroxynonenal and 15-deoxy PGJ2, and various other chemicals. We present here, a review of relevant ROS biology, possible chemical reactions of Cys residues and details of the proteomic strategies employed for rapid, efficient and sensitive identification of diverse and novel PTMs involving reactive Cys residues of redox-sensitive proteins. We propose a new name, ROSics, for the science which describes the principles of mode of action of ROS at molecular levels.
Publisher
WILEY-BLACKWELL
Issue Date
2015-03
Language
English
Article Type
Review
Keywords

EPIDERMAL-GROWTH-FACTOR; TANDEM MASS-SPECTRA; OXYGEN SPECIES ROS; POSTTRANSLATIONAL MODIFICATIONS; HYDROGEN-PEROXIDE; SULFENIC ACID; 15-DEOXY-DELTA(12,14)-PROSTAGLANDIN J(2); REVERSIBLE INACTIVATION; CONJUGATING ENZYMES; LYSINE ACETYLATION

Citation

MASS SPECTROMETRY REVIEWS, v.34, no.2, pp.184 - 208

ISSN
0277-7037
DOI
10.1002/mas.21430
URI
http://hdl.handle.net/10203/195546
Appears in Collection
CH-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 57 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0